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4mba

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[[Image:4mba.jpg|left|200px]]
 
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{{Structure
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==APLYSIA LIMACINA MYOGLOBIN. CRYSTALLOGRAPHIC ANALYSIS AT 1.6 ANGSTROMS RESOLUTION==
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|PDB= 4mba |SIZE=350|CAPTION= <scene name='initialview01'>4mba</scene>, resolution 2.0&Aring;
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<StructureSection load='4mba' size='340' side='right'caption='[[4mba]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>
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<table><tr><td colspan='2'>[[4mba]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aplli Aplli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MBA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MBA FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr>
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|GENE=
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mba OCA], [http://pdbe.org/4mba PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mba RCSB], [http://www.ebi.ac.uk/pdbsum/4mba PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mba ProSAT]</span></td></tr>
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</table>
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'''APLYSIA LIMACINA MYOGLOBIN. CRYSTALLOGRAPHIC ANALYSIS AT 1.6 ANGSTROMS RESOLUTION'''
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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==Overview==
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mb/4mba_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=4mba ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
The crystal structure of the ferric form of myoglobin from the mollusc Aplysia limacina has been refined at 1.6 A resolution, by restrained crystallographic refinement methods. The crystallographic R-factor is 0.19. The tertiary structure of the molecule conforms to the common globin fold, consisting of eight alpha-helices. The N-terminal helix A and helix G deviate significantly from linearity. The distal residue is recognized as Val63 (E7), which, however, does not contact the heme directly. Moreover the sixth (distal) co-ordination position of heme iron is not occupied by a water molecule at neutrality, i.e. below the acid-alkaline transition point of A. limacina myoglobin. The heme group sits in its crevice in the conventional orientation and no signs of heme isomerism are evident. The iron atom is 0.26 A out of the porphyrin plane, with a mean Fe-N (porphyrin) distance of 2.01 A. The co-ordination bond to the proximal histidine has a length of 2.05 A, and forms an angle of 4 degrees with the heme normal. A plane containing the imidazole ring of the proximal His intersects the heme at an angle of 29 degrees with the (porphyrin) 4N-2N direction. Inspection of the structure of pH 9.0 indicates that a hydroxyl ion is bound to the Fe sixth co-ordination position.
The crystal structure of the ferric form of myoglobin from the mollusc Aplysia limacina has been refined at 1.6 A resolution, by restrained crystallographic refinement methods. The crystallographic R-factor is 0.19. The tertiary structure of the molecule conforms to the common globin fold, consisting of eight alpha-helices. The N-terminal helix A and helix G deviate significantly from linearity. The distal residue is recognized as Val63 (E7), which, however, does not contact the heme directly. Moreover the sixth (distal) co-ordination position of heme iron is not occupied by a water molecule at neutrality, i.e. below the acid-alkaline transition point of A. limacina myoglobin. The heme group sits in its crevice in the conventional orientation and no signs of heme isomerism are evident. The iron atom is 0.26 A out of the porphyrin plane, with a mean Fe-N (porphyrin) distance of 2.01 A. The co-ordination bond to the proximal histidine has a length of 2.05 A, and forms an angle of 4 degrees with the heme normal. A plane containing the imidazole ring of the proximal His intersects the heme at an angle of 29 degrees with the (porphyrin) 4N-2N direction. Inspection of the structure of pH 9.0 indicates that a hydroxyl ion is bound to the Fe sixth co-ordination position.
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==About this Structure==
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Aplysia limacina myoglobin. Crystallographic analysis at 1.6 A resolution.,Bolognesi M, Onesti S, Gatti G, Coda A, Ascenzi P, Brunori M J Mol Biol. 1989 Feb 5;205(3):529-44. PMID:2926816<ref>PMID:2926816</ref>
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4MBA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aplysia_limacina Aplysia limacina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MBA OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Aplysia limacina myoglobin. Crystallographic analysis at 1.6 A resolution., Bolognesi M, Onesti S, Gatti G, Coda A, Ascenzi P, Brunori M, J Mol Biol. 1989 Feb 5;205(3):529-44. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2926816 2926816]
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</div>
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[[Category: Aplysia limacina]]
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<div class="pdbe-citations 4mba" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Ascenzi, P.]]
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[[Category: Bolognesi, M.]]
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[[Category: Brunori, M.]]
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[[Category: Coda, A.]]
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[[Category: Gatti, G.]]
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[[Category: Onesti, S.]]
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[[Category: ACE]]
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[[Category: HEM]]
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[[Category: IMD]]
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[[Category: oxygen storage]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:10:17 2008''
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==See Also==
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*[[Myoglobin|Myoglobin]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Aplli]]
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[[Category: Large Structures]]
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[[Category: Ascenzi, P]]
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[[Category: Bolognesi, M]]
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[[Category: Brunori, M]]
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[[Category: Coda, A]]
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[[Category: Gatti, G]]
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[[Category: Onesti, S]]
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[[Category: Oxygen storage]]

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APLYSIA LIMACINA MYOGLOBIN. CRYSTALLOGRAPHIC ANALYSIS AT 1.6 ANGSTROMS RESOLUTION

PDB ID 4mba

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